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MAPK7 — MEF2C
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind_translation Interaction:
MAPK7
—
MEF2C
(experimental interaction detection)
Huang et al., Biochem Biophys Res Commun 2003*
-
IRef Biogrid Interaction:
MAPK7
—
MEF2C
(direct interaction, pull down)
Yang et al., Nucleic Acids Res 1998*
-
IRef Biogrid Interaction:
MAPK7
—
MEF2C
(direct interaction, enzymatic study)
Yang et al., Nucleic Acids Res 1998*
-
IRef Biogrid Interaction:
MAPK7
—
MEF2C
(direct interaction, two hybrid)
Bandyopadhyay et al., Nat Methods 2010
-
IRef Hprd Interaction:
MEF2C
—
MAPK7
(in vitro)
Kato et al., EMBO J 1997*, Yang et al., Nucleic Acids Res 1998*
-
IRef Hprd Interaction:
MEF2C
—
MAPK7
(in vivo)
Kato et al., EMBO J 1997*, Yang et al., Nucleic Acids Res 1998*
-
IRef Intact Interaction:
MAPK7
—
MEF2C
(physical association, two hybrid pooling approach)
Bandyopadhyay et al., Nat Methods 2010
-
IRef Ophid Interaction:
MAPK7
—
MEF2C
(aggregation, confirmational text mining)
Yang et al., Nucleic Acids Res 1998*
-
IRef Ophid Interaction:
MAPK7
—
MEF2C
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Cavanaugh et al., J Neurosci 2001
:
In contrast to ERK1/2,
ERK5 strongly activated the transcriptional activity of myocyte enhancer factor 2C (MEF2C) in pheochromocytoma 12 ( PC12 ) cells and was
required for neurotrophin stimulation of
MEF2C transcription in both PC12 cells and cortical neurons
Ding et al., Stem Cells Dev 2008
:
Nuclear location of
MEF2C , which played a critical role in cardiomyocyte differentiation and could be
activated by
p38MAPK , was stimulated after icariin exposure
Andrews et al., Eur J Immunol 2012
:
The transcription factor
myocyte enhancer factor-2C (MEF2C) is
regulated by both calcineurin and
mitogen activated protein kinase signaling pathways, and is essential for proliferation and survival downstream of BCR engagement in mature B cells
Kato et al., EMBO J 1997
:
BMK1 dramatically
enhances the transactivation activity of
MEF2C by phosphorylating a serine residue at amino acid position 387 in this transcription factor ... Serum is also a potent stimulator of BMK1 induced MEF2C phosphorylation, since a dominant negative form of
BMK1 specifically
inhibits serum induced activation of
MEF2C